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Subunit structure of the reovirus spike

S J Ralph, J D Harvey, A R Bellamy

    Journal of Virology
    |December 1, 1980
    PubMed
    Summary

    Reovirus spike proteins are composed of five lambda 2 polypeptide units. Dimethyl suberimidate cross-linking confirmed this pentameric structure, crucial for viral function.

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    Area of Science:

    • Virology
    • Structural Biology
    • Molecular Biology

    Background:

    • Reoviruses are non-enveloped viruses with a complex outer capsid.
    • The viral spike protein plays a critical role in cell attachment and entry.
    • Understanding the subunit composition of the spike protein is essential for elucidating viral mechanisms.

    Purpose of the Study:

    • To determine the subunit composition of the reovirus spike protein.
    • To investigate the structural organization of the reovirus outer capsid.

    Main Methods:

    • Chemical cross-linking using dimethyl suberimidate, a bifunctional reagent.
    • Analysis of the cross-linked protein complexes using biochemical techniques.

    Main Results:

    • Cross-linking experiments demonstrated that the reovirus spike protein is an aggregate of smaller subunits.
    • Each spike protein was identified as a pentameric assembly.
    • The constituent polypeptide of the spike was identified as lambda 2.

    Conclusions:

    • The reovirus spike protein is structurally organized as a pentamer of lambda 2 polypeptides.
    • This pentameric structure is a fundamental feature of the reovirus outer capsid.
    • The findings provide insights into the molecular architecture of reoviruses.

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